NALP1 (E3F2U) Rabbit mAb #56719
- WB
- IP
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 165 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:100 |
Storage
Protocol
Specificity / Sensitivity
NALP1 (E3F2U) Rabbit mAb recognizes endogenous levels of total NALP1 protein. This antibody recognizes both the 165 kDa full-length NALP1 and the auto-processed 27 kDa C-terminal fragment.
Species Reactivity:
Human
Source / Purification
Monoclonal antibody is produced by immunizing animals with recombinant protein specific to the carboxy terminus of human NALP1 protein.
Background
NALP1 (DEFCAP/NAC/CARD7) is an NLR (Nod-like receptor) family member that has been implicated in the regulation of apoptosis and inflammatory responses (1-5). Structurally, NALP contains an amino-terminal PYRIN domain, followed by a nucleotide-binding site (NBS), a leucine-rich repeat region (LRR), and a carboxy-terminal CARD domain. NALP1 interacts strongly with caspase-2 and weakly with caspase-9, and induces apoptosis when overexpressed (3). Similar to a related Ced-4 family member Apaf-1, it was also shown to be involved in cytochrome c-dependent caspase activation (2). It has also been shown to be part of the "inflammasome" comprised of caspase-1, caspase-5, and Pycard/ASC, which is critical in the processing of pro-inflammatory cytokines like IL-1β (6). Two major isoforms were identified for NALP1, which differ in a 44 amino acid region within the LRR (3). In addition, like NALP3, a short NALP1 isoform lacking the LRR (NALP1s) likely exists (7). Polymorphisms in NALP1 have been associated with autoimmune diseases (8) and susceptibility to toxins (9).
NALP1 is autoproteolytically processed into a large N-terminal and a small C-terminal fragment, which are non-covalently associated. Upon activation, the C-terminal is released and forms inflammasomes with other proteins (10-12).
- Bertin, J. and DiStefano, P.S. (2000) Cell Death Differ. 7, 1273-1274.
- Chu, Z.L. et al. (2001) J. Biol. Chem. 276, 9239-9245.
- Hlaing, T. et al. (2001) J. Biol. Chem. 276, 9230-9238.
- Martinon, F. et al. (2001) Curr. Biol. 11, R118-R120.
- Fritz, J.H. et al. (2006) Nat. Immunol. 7, 1250-1257.
- Martinon, F. et al. (2002) Mol. Cell 10, 417-426.
- Kummer, J.A. et al. (2007) J. Histochem. Cytochem. 55, 443-452.
- Jin, Y. et al. (2007) N. Engl. J. Med. 356, 1216-1225.
- Boyden, E.D. and Dietrich, W.F. (2006) Nat. Genet. 38, 240-244.
- D'Osualdo, A. et al. (2011) PLoS One 6, e27396.
- Robert Hollingsworth, L. et al. (2021) Nat Commun 12, 189.
- Gong, Q. et al. (2021) Nat Commun 12, 188.
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